Proteinase K from Tritirachium album Limber
نویسندگان
چکیده
منابع مشابه
Comparative Studies on the Interaction of Proteinase-K with Nano-CuO and Copper Ions
The interaction of copper oxide nanoparticles and copper ions and proteinase K from Tritirachium album Limber has been investigated employing UV spectroscopy and kinetics measurements. The aim of this study was to evaluate the effect of nanoparticles of CuO for proteinase K. In this paper we compare the effect of copper oxide nanoparticles with the effect of copper ions on proteinase K sta...
متن کاملComparative Studies on the Interaction of Proteinase-K with Nano-CuO and Copper Ions
The interaction of copper oxide nanoparticles and copper ions and proteinase K from Tritirachium album Limber has been investigated employing UV spectroscopy and kinetics measurements. The aim of this study was to evaluate the effect of nanoparticles of CuO for proteinase K. In this paper we compare the effect of copper oxide nanoparticles with the effect of copper ions on proteinase K stabilit...
متن کاملCrystal structure of calcium-free proteinase K at 1.5-A resolution.
Proteinase K from the fungus Tritirachium album Limber binds two Ca2+ ions, one strongly (Ca 1) and the other weakly (Ca 2). Removal of these cations reduces the stability of proteinase K as shown by thermal denaturation, but the proteolytic activity is unchanged. The x-ray structures of native and Ca(2+)-free proteinase K at 1.5-A resolution show that there are no cuts in the polypeptide backb...
متن کاملcomparative studies on the interaction of proteinase-k with nano-cuo and copper ions
the interaction of copper oxide nanoparticles and copper ions and proteinase k from tritirachium album limber has been investigated employing uv spectroscopy and kinetics measurements. the aim of this study was to evaluate the effect of nanoparticles of cuo for proteinase k. in this paper we compare the effect of copper oxide nanoparticles with the effect of copper ions on proteinase k stabilit...
متن کاملMercury induced modifications in the stereochemistry of the active site through Cys-73 in a serine protease--crystal structure of the complex of a partially modified proteinase K with mercury at 1.8 A resolution.
Proteinese K (PK) isolated from Tritirachium album Limber was crystallized with HgCl2 in excess, under microgravity conditions. The intensity data were collected at 4 degrees C to 1.8 A resolution and the final R-factor after refinement for all the reflections was 0.164. Mercury has been found at two sites with partial occupancies (0.4 and 0.6) which are at distances of 2.48 A and 2.58 A respec...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1974
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1974.tb03671.x